Glycoconjugate Journal

, Volume 23, Issue 1–2, pp 115–125 | Cite as

Search for additional influenza virus to cell interactions

  • E. M. Rapoport
  • L. V. Mochalova
  • H.-J. Gabius
  • J. Romanova
  • N. V. Bovin


Sialyl oligosaccharides have long been considered to be the sole receptors for influenza virus. However, according to [1] some viruses are able to grow in sialic-free MDCK cells. Here we attempted to reveal a possible second, non-sialic receptor, hypothesizing the involvement of additional carbohydrate lectin recognition in influenza virus reception process, first of all in situations when a lectin of the host cell could recognize the viral carbohydrate ligand. We tested the presence of galactose- and sialic acid-binding lectins, as well as mannoside- and sulfo-N-acetyllactosamine-recognizing properties of MDCK and Vero cells using polyacrylamide neoglycoconjugates and antibodies. MDCK cells bind galactoside probes stronger than Vero cells, whereas Vero cells bind preferentially sialoside, mannoside and various sulfo-oligosaccharide probes. The probing of viruses with the neoglycoconjugates revealed specific 6′-HSO 3 LacNAc (but not other sulfated oligosaccharides) binding property of A and B human strains. Affinity of 6′-HSO 3 LacNAc probe was comparable with affinity of 6′-SiaLac probe but the binding was not inhibited by the sialooligosaccharide.


Galectins Glycoconjugates Influenza virus Hemagglutinin Siglecs 



baby hamster kidney cells


biotin residue


bovine serum albumin


fetal bovine serum


fluorescein isothiocyanate


fluorescein residue




mannose-binding protein


Madin-Darby bovine kidney cells


Madin-Darby canine kidney cells








phosphate buffered saline


PBS containing 0.2% BSA


receptor binding site


surfactant protein


mono- or oligosaccharide residue










α-N-acetylneuraminic acid





Man 3


A tri


A tetra


B tri


SiaLe x



(GlcNAcβ1-2Manα1-) 2-3,6-Manβ1-4GlcNAcβ1-4GlcNAc


(Neu5Acα2-6Galβ1-4GlcNAcβ1- 2Manα1-)2-3, 6-Manβ1-4GlcNAcβ1- 4GlcNAc






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Copyright information

© Springer Science + Business Media, LLC 2006

Authors and Affiliations

  • E. M. Rapoport
    • 1
  • L. V. Mochalova
    • 1
  • H.-J. Gabius
    • 2
  • J. Romanova
    • 3
  • N. V. Bovin
    • 1
  1. 1.Shemyakin & Ovchinnikov Institute of Bioorganic ChemistryRussian Academy of SciencesMoscowRussia
  2. 2.Institut für Physiologische Chemie, Tierärztliche FakultätLudwig-Maximilians-UniversitätMunichGermany
  3. 3.Institute of Applied MicrobiologyUniversity of Natural Resources and Applied Life SciencesViennaAustria

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